1989
DOI: 10.1016/0006-291x(89)91794-4
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Characterization of a Mr 25,000 basic fibroblast growth factor form in adult, regenerating, and fetal rat liver

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Cited by 42 publications
(29 citation statements)
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“…The 148 amino acid form could not result from an internal initiation of the translation since there is no methionine or other unusual initiation codon near the cleavage site (SIT"TLP). The same truncated form was also observed in extracts of eukaryotic cells producing the 210FGF-2 form (data not shown) and was described as artefactual degradation occurring during storage of tissues at -20°C [28,33]. Futhermore, we and others never identified such a maturation product after the 155FGF-2 form production suggesting that the processing recognition site is not fully present in the 155 amino acid form [15,18,19].…”
Section: Pur$cation Of the R21ofgf-2supporting
confidence: 61%
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“…The 148 amino acid form could not result from an internal initiation of the translation since there is no methionine or other unusual initiation codon near the cleavage site (SIT"TLP). The same truncated form was also observed in extracts of eukaryotic cells producing the 210FGF-2 form (data not shown) and was described as artefactual degradation occurring during storage of tissues at -20°C [28,33]. Futhermore, we and others never identified such a maturation product after the 155FGF-2 form production suggesting that the processing recognition site is not fully present in the 155 amino acid form [15,18,19].…”
Section: Pur$cation Of the R21ofgf-2supporting
confidence: 61%
“…Analysis of an extended hepatoma FGF-2 cDNA revealed unusual start codons [22]: proteins result from an alternative initiation of translation at an AUG (155FGF-2, 155 amino acids: 18 kDa) or at three inframe upstream CUGs (210FGF-2, 210 amino acids: 24 kDa, 201 amino acids: 22.5 kDa and 196 amino *Corresponding author. Fax: (33) 6226-4012. acids: 22 kDa) [22,23]. The high molecular weight forms of FGF-2 contain a glycine-arginine-rich domain where arginines can be dimethylated [24].…”
Section: Introductionmentioning
confidence: 99%
“…Hep ato cellular production of VEGF peaks 48-72 hours after hepatectomy, 20 as mitogens for hepatocytes FGF-2 are overexpressed in the regenerating liver. 21,22 It has been reported that FGF-2 stimulates the regeneration of the extracellular matrix after liver injury and regulates proliferation and migration of hepatocytes in vitro. 23,24 In the regenerating liver, FGF-2 seems to be primarily produced in hepatic stellate cells acting on the sinusoids.…”
Section: Discussionmentioning
confidence: 99%
“…Although mRNA levels are very low, resting adult livers contain abundant reserves of FGF1 and FGF2 protein at levels higher than most other tissues (12). FGF1 and FGF2 mRNAs increase in response to partial hepatectomy or damage (13)(14)(15). Other FGF homologues have been reported in liver, but their significance, cellular target, and physiologic role are unclear (16).…”
Section: Introductionmentioning
confidence: 99%